Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004553 | molecular_function | hydrolase activity, hydrolyzing O-glycosyl compounds |
| A | 0004556 | molecular_function | alpha-amylase activity |
| A | 0005509 | molecular_function | calcium ion binding |
| A | 0005576 | cellular_component | extracellular region |
| A | 0005975 | biological_process | carbohydrate metabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016798 | molecular_function | hydrolase activity, acting on glycosyl bonds |
| A | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1483 |
| Chain | Residue |
| A | ASP162 |
| A | ALA182 |
| A | ASP184 |
| A | ASP203 |
| A | HOH2185 |
| A | HOH2199 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CA A 1484 |
| Chain | Residue |
| A | HIS236 |
| A | HOH2110 |
| A | ASP105 |
| A | ASP195 |
| A | ASP201 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CA A 1485 |
| Chain | Residue |
| A | GLY301 |
| A | PHE303 |
| A | SER404 |
| A | ASP405 |
| A | ASP428 |
| A | HOH2298 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1486 |
| Chain | Residue |
| A | GLN128 |
| A | GLN128 |
| A | GLN128 |
| A | GLN128 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 1487 |
| Chain | Residue |
| A | LYS177 |
| A | LYS177 |
| A | HOH2200 |
| A | HOH2200 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1491 |
| Chain | Residue |
| A | ASP162 |
| A | ASP184 |
| A | ASP195 |
| A | ASP201 |
| A | LEU202 |
| site_id | AC7 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1492 |
| Chain | Residue |
| A | HOH2143 |
| A | HOH2144 |
| A | HOH2145 |
| A | HOH2155 |
| A | HOH2156 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NA A 1490 |
| Chain | Residue |
| A | ASP232 |
| A | GLU262 |
| A | HOH2241 |
| A | HOH2242 |
| A | HOH2261 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE GLY A 1488 |
| Chain | Residue |
| A | TYR134 |
| A | HOH2134 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GLY A 1489 |
| Chain | Residue |
| A | GLY109 |
| A | TYR199 |
| A | HOH2186 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Nucleophile"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton donor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"11226887","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1HVX","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Site: {"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000250"}]} |
